Caspase-1 is activated in neural cells and tissue with amyotrophic lateral sclerosis-associated mutations in copper-zinc superoxide dismutase

Superoxide Dismutase ◽

Neural Cells ◽

Caspase 1 ◽

Copper Zinc ◽

Dysregulation of intracellular copper trafficking pathway in a mouse model of mutant copper/zinc superoxide dismutase-linked familial amyotrophic lateral sclerosis

Journal of Neurochemistry ◽

10.1111/j.1471-4159.2009.06310.x ◽

2009 ◽

Vol 111 (1) ◽

pp. 181-191 ◽

Cited By ~ 38

Author(s):

Eiichi Tokuda ◽

Eriko Okawa ◽

Shin-ichi Ono

Keyword(s):

Superoxide Dismutase ◽

Copper Trafficking ◽

Trafficking Pathway ◽

Copper Zinc ◽

Lateral Sclerosis ◽

Intracellular Copper

Human Copper-Zinc Superoxide Dismutase and Familial Amyotrophic Lateral Sclerosis

Protein Misfolding, Aggregation, and Conformational Diseases - Protein Reviews ◽

10.1007/978-0-387-36534-3_16 ◽

2007 ◽

pp. 327-344 ◽

Cited By ~ 1

Author(s):

Ahmad Galaleldeen ◽

P. John Hart

Keyword(s):

Superoxide Dismutase ◽

Copper Zinc ◽

Copper/zinc superoxide dismutase mRNA levels are increased in sporadic amyotrophic lateral sclerosis motorneurons

Brain Research ◽

10.1016/0006-8993(94)90892-3 ◽

1994 ◽

Vol 659 (1-2) ◽

pp. 272-276 ◽

Cited By ~ 35

Author(s):

Catherine Bergeron ◽

Siham Muntasser ◽

Martin J. Somerville ◽

Luitgard Weyer ◽

Maire E. Percy

Keyword(s):

Superoxide Dismutase ◽

Sporadic Amyotrophic Lateral Sclerosis ◽

Mrna Levels ◽

Copper Zinc ◽

Interaction of Amyotrophic Lateral Sclerosis (ALS)-related Mutant Copper-Zinc Superoxide Dismutase with the Dynein-Dynactin Complex Contributes to Inclusion Formation

Journal of Biological Chemistry ◽

10.1074/jbc.m800276200 ◽

2008 ◽

Vol 283 (33) ◽

pp. 22795-22805 ◽

Cited By ~ 37

Author(s):

Anna-Lena Ström ◽

Ping Shi ◽

Fujian Zhang ◽

Jozsef Gal ◽

Renee Kilty ◽

...

Keyword(s):

Superoxide Dismutase ◽

Inclusion Formation ◽

Copper Zinc ◽

Dynactin Complex ◽

Reduced net charge and heterogeneity of pIisoforms in familial amyotrophic lateral sclerosis mutants of copper/zinc superoxide dismutase

Electrophoresis ◽

10.1002/elps.201500187 ◽

2015 ◽

Vol 36 (19) ◽

pp. 2482-2488 ◽

Cited By ~ 9

Author(s):

Stéphane Roudeau ◽

Sylviane Chevreux ◽

Asuncion Carmona ◽

Richard Ortega

Keyword(s):

Superoxide Dismutase ◽

Net Charge ◽

Copper Zinc ◽

Dimerization, Oligomerization, and Aggregation of Human Amyotrophic Lateral Sclerosis Copper/Zinc Superoxide Dismutase 1 Protein Mutant Forms in Live Cells

Journal of Biological Chemistry ◽

10.1074/jbc.m113.542613 ◽

2014 ◽

Vol 289 (21) ◽

pp. 15094-15103 ◽

Cited By ~ 31

Author(s):

Jiho Kim ◽

Honggun Lee ◽

Joo Hyun Lee ◽

Do-yoon Kwon ◽

Auguste Genovesio ◽

...

Keyword(s):

Superoxide Dismutase ◽

Live Cells ◽

Superoxide Dismutase 1 ◽

Copper Zinc ◽

Mutant Forms ◽

Mutant copper-zinc superoxide dismutase associated with amyotrophic lateral sclerosis binds to adenine/uridine-rich stability elements in the vascular endothelial growth factor 3′-untranslated region

Journal of Neurochemistry ◽

10.1111/j.1471-4159.2008.05856.x ◽

2009 ◽

Vol 108 (4) ◽

pp. 1032-1044 ◽

Cited By ~ 22

Author(s):

Xuelin Li ◽

Liang Lu ◽

Donald J. Bush ◽

Xiaowen Zhang ◽

Lei Zheng ◽

...

Keyword(s):

Vascular Endothelial Growth Factor ◽

Superoxide Dismutase ◽

Untranslated Region ◽

Vascular Endothelial ◽

Copper Zinc ◽

Endothelial Growth Factor ◽

The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease)

JBIC Journal of Biological Inorganic Chemistry ◽

10.1007/s00775-003-0447-6 ◽

2003 ◽

Vol 8 (4) ◽

pp. 373-380 ◽

Cited By ~ 43

Author(s):

Soshanna Zittin Potter ◽

Joan Selverstone Valentine

Keyword(s):

Superoxide Dismutase ◽

Copper Zinc ◽

Lou Gehrig’S Disease ◽

Lou Gehrig's Disease ◽

Copper-Zinc Superoxide Dismutase and Familial Amyotrophic Lateral Sclerosis

Neurodegenerative Diseases and Metal Ions ◽

10.1002/0470028114.ch8 ◽

2006 ◽

pp. 179-205

Author(s):

Lisa J. Whitson ◽

P. John Hart

Keyword(s):

Superoxide Dismutase ◽

Copper Zinc ◽

Faculty Opinions recommendation of Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosis.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1012344.185335 ◽

2003 ◽

Author(s):

Elizabeth Theil

Keyword(s):

Superoxide Dismutase ◽

Nmr Spectroscopy ◽

Dynamic Properties ◽

Copper Zinc ◽